Structure and mechanism of DNA topoisomerase II

Berger, James M.
Gamblin, Steven J.
Harrison, Stephen C.
Wang, James C.

Department of Molecular and Cellular Biology and (Harrison) Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts 02138, USA.
(Berger, Gamblin) Present addresses: Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, Massachusetts 02142, USA (J.M.B.); National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK (S.J.G.).

Nature 379(6562):p 225-232, January 18, 1996.

The crystal structure of a large fragment of yeast type II DNA topoisomerase reveals a heart-shaped dimeric protein with a large central hole. It provides a molecular model of the enzyme as an ATP-modulated clamp with two sets of jaws at opposite ends, connected by multiple joints. An enzyme with bound DNA can admit a second DNA duplex through one set of jaws, transport it through the cleaved first duplex, and expel it through the other set of jaws.